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Render Timestamp: 2024-11-21T13:58:28.785Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-10-16 17:30:11.889
Product last modified at: 2024-11-07T15:15:16.723Z
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PDP - Template Name: Antibody Sampler Kit
PDP - Template ID: *******4a3ef3a

Matrix Remodeling Antibody Sampler Kit #73959

    Product Information

    Product Description

    The Matrix Remodeling Antibody Sampler Kit provides an economical means of detecting different MMPs and TIMPs using the specific corresponding antibodies. The kit contains enough antibody to perform at least two western blot experiments with each primary antibody.

    Background

    Matrix remodeling is mainly controlled by MMPs and TIMPs. The matrix metalloproteinase (MMP) family of proteases are a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, matrix structural proteins, and other proteases (1, 2). Among the family members, MMP-2, MMP-3, MMP-7, MMP-9, and MMP14 (MT1-MMP) have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (3). MMP activity is regulated by mechanisms of both transcriptional control and post translational protein processing. Once synthesized, MMPs exist as latent proenzymes. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full-length protein (4). MMP activity can be inhibited through its binding to endogenously expressed TIMPs. TIMPs are members of the family of tissue inhibitors of matrix metalloproteinases that include TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding MMPs and chelating their zinc cofactor at the catalytic site to inhibit the proteinase function (5,6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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